2011
DOI: 10.1016/j.bbadis.2011.01.012
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Analysis of the mitochondrial proteome in multiple sclerosis cortex

Abstract: Mitochondrial dysfunction has been proposed to play a role in the neuropathology of multiple sclerosis (MS). Previously, we reported significant alterations in the transcription of nuclear-encoded electron transport chain genes in MS and confirmed translational alterations for components of Complexes I and III that resulted in reductions in their activity. To more thoroughly and efficiently elucidate potential alterations in the expression of mitochondrial and related proteins, we have characterized the mitoch… Show more

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Cited by 104 publications
(95 citation statements)
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“…Intracellular hemoglobin shows remarkable compartmentalization; it concentrates to the mitochondria, where it shows a particularly close association with mitochondrial complex I. It is interesting to note that a recent proteomic analysis of control brains and brains from multiple sclerosis patients has identified the mitochondrial localization of the hemoglobin β chain (30). The functional consequence of mitochondrial hemoglobin remains to be further elucidated; based on the current results, we speculate that it may either contribute to a specific mitochondrial protection (for example, against mitochondrial oxidative stress), or it may play a more specific role in the regulation of mitochondrial electron transport; the latter hypothesis is supported by our extracellular flux analysis findings indicating an increased basal and FCCP-uncoupled maximal rate of mitochondrial respiration in cells with increased mitochondrial hemoglobin content.…”
Section: Discussionmentioning
confidence: 99%
“…Intracellular hemoglobin shows remarkable compartmentalization; it concentrates to the mitochondria, where it shows a particularly close association with mitochondrial complex I. It is interesting to note that a recent proteomic analysis of control brains and brains from multiple sclerosis patients has identified the mitochondrial localization of the hemoglobin β chain (30). The functional consequence of mitochondrial hemoglobin remains to be further elucidated; based on the current results, we speculate that it may either contribute to a specific mitochondrial protection (for example, against mitochondrial oxidative stress), or it may play a more specific role in the regulation of mitochondrial electron transport; the latter hypothesis is supported by our extracellular flux analysis findings indicating an increased basal and FCCP-uncoupled maximal rate of mitochondrial respiration in cells with increased mitochondrial hemoglobin content.…”
Section: Discussionmentioning
confidence: 99%
“…Autophagy maintains the architecture of mitochondria, restores their function, and prevents their dysfunction, which are critical for cell survival and the pathogenesis of MS [21][22][23] . In MS, the decreased expression of cytochrome c oxidase subunit 5b may impair the function of mitochondria [24] . Dysfunction of mitochondria produces reactive oxygen species (ROS), which contribute to demyelination and axonal loss [25] .…”
mentioning
confidence: 99%
“…The potential for utilization of protein microarrays in analysis of renal mitochondria could be in high throughput monitoring of selected pathways by analysis of multiple, predefined set of proteins. Arrays based on mass spectrometric detection of proteins bound to affinity surfaces (surface-enhanced laser desorption and ionization, SELDI) have been used for analysis of brain mitochondria 66,67 . Chips with wide range of surfaces are available for SELDI.…”
Section: Methods For Analysis Of Mitochondrial Proteomementioning
confidence: 99%